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Q8DXM9

- GSHAB_STRA5

UniProt

Q8DXM9 - GSHAB_STRA5

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Protein

Glutathione biosynthesis bifunctional protein GshAB

Gene

gshAB

Organism
Streptococcus agalactiae serotype V (strain ATCC BAA-611 / 2603 V/R)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

Synthesizes glutathione from L-glutamate and L-cysteine via gamma-L-glutamyl-L-cysteine.

Catalytic activityi

ATP + L-glutamate + L-cysteine = ADP + phosphate + gamma-L-glutamyl-L-cysteine.UniRule annotation
ATP + gamma-L-glutamyl-L-cysteine + glycine = ADP + phosphate + glutathione.UniRule annotation

Cofactori

Mg2+By similarity, Mn2+By similarityNote: Binds 2 magnesium or manganese ions per subunit.By similarity

Enzyme regulationi

Inhibited by L-buthionine-S-sulfoximine (L-S-BSO).

Kineticsi

  1. KM=22 mM for L-glutamate
  2. KM=156 µM for L-cysteine
  3. KM=8.2 mM for alpha-L-aminobutyrate
  4. KM=64 µM for ATP (in the reaction with gamma-GCS)
  5. KM=5.9 mM for gamma-L-glutamyl-L-cysteine
  6. KM=11.5 mM for gamma-L-glutamyl-L-alpha-aminobutyrate
  7. KM=6.3 mM for glycine
  8. KM=420 µM for ATP (in the reaction with GS)

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi696 – 6961Magnesium or manganese 1UniRule annotation
Metal bindingi717 – 7171Magnesium or manganese 1UniRule annotation
Metal bindingi717 – 7171Magnesium or manganese 2UniRule annotation
Metal bindingi719 – 7191Magnesium or manganese 2UniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi516 – 57459ATPUniRule annotationAdd
BLAST

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-HAMAP
  2. glutamate-cysteine ligase activity Source: UniProtKB-HAMAP
  3. glutathione synthase activity Source: UniProtKB-HAMAP
  4. magnesium ion binding Source: UniProtKB-HAMAP
  5. manganese ion binding Source: UniProtKB-HAMAP
Complete GO annotation...

Keywords - Molecular functioni

Ligase

Keywords - Biological processi

Glutathione biosynthesis

Keywords - Ligandi

ATP-binding, Magnesium, Manganese, Metal-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciSAGA208435:GHVY-1917-MONOMER.
BRENDAi6.3.2.3. 5917.
SABIO-RKQ8DXM9.
UniPathwayiUPA00142; UER00209.
UPA00142; UER00210.

Names & Taxonomyi

Protein namesi
Recommended name:
Glutathione biosynthesis bifunctional protein GshABUniRule annotation
Alternative name(s):
Gamma-GCS-GSUniRule annotation
Short name:
GCS-GSUniRule annotation
Including the following 2 domains:
Glutamate--cysteine ligaseUniRule annotation (EC:6.3.2.2UniRule annotation)
Alternative name(s):
Gamma-ECSUniRule annotation
Short name:
GCSUniRule annotation
Gamma-glutamylcysteine synthetaseUniRule annotation
Glutathione synthetaseUniRule annotation (EC:6.3.2.3UniRule annotation)
Alternative name(s):
GSH synthetaseUniRule annotation
Short name:
GSUniRule annotation
Short name:
GSH-SUniRule annotation
Short name:
GSHaseUniRule annotation
Glutathione synthaseUniRule annotation
Gene namesi
Name:gshABUniRule annotation
Synonyms:gshFUniRule annotation
Ordered Locus Names:SAG1821
OrganismiStreptococcus agalactiae serotype V (strain ATCC BAA-611 / 2603 V/R)
Taxonomic identifieri208435 [NCBI]
Taxonomic lineageiBacteriaFirmicutesBacilliLactobacillalesStreptococcaceaeStreptococcus
ProteomesiUP000000821: Chromosome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 750750Glutathione biosynthesis bifunctional protein GshABPRO_0000192559Add
BLAST

Interactioni

Subunit structurei

Monomer.Curated

Protein-protein interaction databases

STRINGi208435.SAG1821.

Structurei

Secondary structure

1
750
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi7 – 93Combined sources
Beta strandi19 – 3113Combined sources
Turni32 – 354Combined sources
Beta strandi44 – 463Combined sources
Turni49 – 513Combined sources
Beta strandi53 – 6715Combined sources
Beta strandi71 – 733Combined sources
Helixi74 – 9118Combined sources
Beta strandi96 – 983Combined sources
Beta strandi101 – 1033Combined sources
Turni109 – 1113Combined sources
Helixi120 – 13314Combined sources
Helixi136 – 1394Combined sources
Beta strandi143 – 1497Combined sources
Helixi151 – 16111Combined sources
Helixi166 – 19126Combined sources
Beta strandi199 – 2013Combined sources
Turni206 – 2083Combined sources
Beta strandi212 – 2143Combined sources
Beta strandi217 – 2215Combined sources
Helixi234 – 24310Combined sources
Turni246 – 2483Combined sources
Helixi253 – 2553Combined sources
Beta strandi259 – 2646Combined sources
Turni268 – 2747Combined sources
Beta strandi278 – 2814Combined sources
Helixi296 – 31116Combined sources
Helixi318 – 33417Combined sources
Helixi347 – 36115Combined sources
Helixi365 – 37915Combined sources
Helixi381 – 3833Combined sources
Helixi385 – 3928Combined sources
Helixi399 – 41315Combined sources
Helixi421 – 4233Combined sources
Helixi428 – 44013Combined sources
Beta strandi443 – 4475Combined sources
Beta strandi449 – 4513Combined sources
Beta strandi453 – 4586Combined sources
Beta strandi461 – 4666Combined sources
Turni467 – 4693Combined sources
Helixi477 – 4815Combined sources
Turni482 – 4843Combined sources
Helixi486 – 4949Combined sources
Turni507 – 5104Combined sources
Helixi511 – 5177Combined sources
Beta strandi518 – 5214Combined sources
Beta strandi523 – 5275Combined sources
Beta strandi532 – 5354Combined sources
Beta strandi537 – 5415Combined sources
Helixi545 – 55814Combined sources
Beta strandi560 – 5667Combined sources
Beta strandi570 – 5789Combined sources
Beta strandi581 – 5899Combined sources
Beta strandi592 – 5943Combined sources
Helixi601 – 6088Combined sources
Beta strandi614 – 6185Combined sources
Beta strandi621 – 6233Combined sources
Helixi629 – 6379Combined sources
Beta strandi651 – 6544Combined sources
Turni660 – 6634Combined sources
Beta strandi665 – 6684Combined sources
Turni670 – 6723Combined sources
Helixi675 – 68713Combined sources
Beta strandi694 – 7007Combined sources
Beta strandi702 – 7043Combined sources
Turni708 – 7114Combined sources
Beta strandi714 – 7218Combined sources
Helixi725 – 7284Combined sources
Beta strandi731 – 7333Combined sources
Helixi739 – 7468Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3LN6X-ray2.95A1-750[»]
ProteinModelPortaliQ8DXM9.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini489 – 747259ATP-graspUniRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 333333Glutamate--cysteine ligaseAdd
BLAST

Sequence similaritiesi

In the N-terminal section; belongs to the glutamate--cysteine ligase type 1 family. Type 2 subfamily.UniRule annotation
Contains 1 ATP-grasp domain.UniRule annotation

Phylogenomic databases

eggNOGiCOG1181.
HOGENOMiHOG000156471.
KOiK01919.
OMAiHVEYVKN.
OrthoDBiEOG6BKJ7H.

Family and domain databases

Gene3Di3.30.470.20. 1 hit.
HAMAPiMF_00782. Glut_biosynth.
InterProiIPR011761. ATP-grasp.
IPR013816. ATP_grasp_subdomain_2.
IPR007370. Glu_cys_ligase.
IPR006335. Glut_biosynth.
[Graphical view]
PfamiPF04262. Glu_cys_ligase. 1 hit.
[Graphical view]
TIGRFAMsiTIGR01435. glu_cys_lig_rel. 1 hit.
PROSITEiPS50975. ATP_GRASP. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q8DXM9-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MIIDRLLQRS HSHLPILQAT FGLERESLRI HQPTQRVAQT PHPKTLGSRN
60 70 80 90 100
YHPYIQTDYS EPQLELITPI AKDSQEAIRF LKAISDVAGR SINHDEYLWP
110 120 130 140 150
LSMPPKVREE DIQIAQLEDA FEYDYRKYLE KTYGKLIQSI SGIHYNLGLG
160 170 180 190 200
QELLTSLFEL SQADNAIDFQ NQLYMKLSQN FLRYRWLLTY LYGASPVAEE
210 220 230 240 250
DFLDQKLNNP VRSLRNSHLG YVNHKDIRIS YTSLKDYVND LENAVKSGQL
260 270 280 290 300
IAEKEFYSPV RLRGSKACRN YLEKGITYLE FRTFDLNPFS PIGITQETVD
310 320 330 340 350
TVHLFLLALL WIDSSSHIDQ DIKEANRLND LIALSHPLEK LPNQAPVSDL
360 370 380 390 400
VDAMQSVIQH FNLSPYYQDL LESVKRQIQS PELTVAGQLL EMIEGLSLET
410 420 430 440 450
FGQRQGQIYH DYAWEAPYAL KGYETMELST QLLLFDVIQK GVNFEVLDEQ
460 470 480 490 500
DQFLKLWHNS HIEYVKNGNM TSKDNYIVPL AMANKVVTKK ILDEKHFPTP
510 520 530 540 550
FGDEFTDRKE ALNYFSQIQD KPIVVKPKST NFGLGISIFK TSANLASYEK
560 570 580 590 600
AIDIAFTEDS AILVEEYIEG TEYRFFVLEG DCIAVLLRVA ANVVGDGIHT
610 620 630 640 650
ISQLVKLKNQ NPLRGYDHRS PLEVIELGEV EQLMLEQQGY TVNSIPPEGT
660 670 680 690 700
KIELRRNSNI STGGDSIDVT NTMDPTYKQL AAEMAEAMGA WVCGVDLIIP
710 720 730 740 750
NATQAYSKDK KNATCIELNF NPLMYMHTYC QEGPGQSITP RILAKLFPEL
Length:750
Mass (Da):85,603
Last modified:March 1, 2003 - v1
Checksum:i97829C2C5B44174A
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE009948 Genomic DNA. Translation: AAN00684.1.
RefSeqiNP_688811.1. NC_004116.1.

Genome annotation databases

EnsemblBacteriaiAAN00684; AAN00684; SAG1821.
GeneIDi1014630.
KEGGisag:SAG1821.
PATRICi19630489. VBIStrAga72745_1829.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AE009948 Genomic DNA. Translation: AAN00684.1 .
RefSeqi NP_688811.1. NC_004116.1.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3LN6 X-ray 2.95 A 1-750 [» ]
ProteinModelPortali Q8DXM9.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 208435.SAG1821.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

EnsemblBacteriai AAN00684 ; AAN00684 ; SAG1821 .
GeneIDi 1014630.
KEGGi sag:SAG1821.
PATRICi 19630489. VBIStrAga72745_1829.

Phylogenomic databases

eggNOGi COG1181.
HOGENOMi HOG000156471.
KOi K01919.
OMAi HVEYVKN.
OrthoDBi EOG6BKJ7H.

Enzyme and pathway databases

UniPathwayi UPA00142 ; UER00209 .
UPA00142 ; UER00210 .
BioCyci SAGA208435:GHVY-1917-MONOMER.
BRENDAi 6.3.2.3. 5917.
SABIO-RK Q8DXM9.

Family and domain databases

Gene3Di 3.30.470.20. 1 hit.
HAMAPi MF_00782. Glut_biosynth.
InterProi IPR011761. ATP-grasp.
IPR013816. ATP_grasp_subdomain_2.
IPR007370. Glu_cys_ligase.
IPR006335. Glut_biosynth.
[Graphical view ]
Pfami PF04262. Glu_cys_ligase. 1 hit.
[Graphical view ]
TIGRFAMsi TIGR01435. glu_cys_lig_rel. 1 hit.
PROSITEi PS50975. ATP_GRASP. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: ATCC BAA-611 / 2603 V/R.
  2. "Glutathione synthesis in Streptococcus agalactiae. One protein accounts for gamma-glutamylcysteine synthetase and glutathione synthetase activities."
    Janowiak B.E., Griffith O.W.
    J. Biol. Chem. 280:11829-11839(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION.
    Strain: ATCC BAA-611 / 2603 V/R.

Entry informationi

Entry nameiGSHAB_STRA5
AccessioniPrimary (citable) accession number: Q8DXM9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 24, 2004
Last sequence update: March 1, 2003
Last modified: November 26, 2014
This is version 80 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programProkaryotic Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Multifunctional enzyme, Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3